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Literature summary extracted from

  • Varsani, L.; Cui, T.; Rangarajan, M.; Hartley, B.S.; Goldberg, J.; Collyer, C.; Blow, D.M.
    Arthrobacter D-xylose isomerase: protein-engineered subunit interfaces (1993), Biochem. J., 291, 575-583.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
5.3.1.5 wild-type and mutant enzymes, expression in Escherichia coli Arthrobacter sp.

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
5.3.1.5 wild-type and mutant enzymes Arthrobacter sp.

Protein Variants

EC Number Protein Variants Comment Organism
5.3.1.5 Y253C a Tyr253 mutant in which a disulfide bridge is introduced at the A-B subunit interface shows reduced thermostability, that is identical in both oxidized and reduced forms and also reduced stability in urea. X-ray-crystallographic analysis of the Mn2+-xylitol form of oxidized Y253C shows a changed conformation of Glu185 and also alternative conformations for Asp254, which is a ligand to the site 2 metal ion. With fructose, Mg2+-Y253C has a similar Km to that of the wild-type, and its maximal velocity is also similar below pH 6.4, but declines thereafter. In presence of Co2+, Y253C has lower activity than wild-type at all pH values, but its activity also declines at alkaline pH Arthrobacter sp.

Organism

EC Number Organism UniProt Comment Textmining
5.3.1.5 Arthrobacter sp.
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
5.3.1.5
-
 Arthrobacter sp.

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
5.3.1.5 D-Xylose
-
 Arthrobacter sp. D-Xylulose
-
 ?